ID A0A0S7C2M1_9BACT Unreviewed; 279 AA.
AC A0A0S7C2M1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=deoxyribose-phosphate aldolase {ECO:0000256|ARBA:ARBA00012515};
DE EC=4.1.2.4 {ECO:0000256|ARBA:ARBA00012515};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|ARBA:ARBA00032755};
DE AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|ARBA:ARBA00031814};
GN ORFNames=TBC1_111826 {ECO:0000313|EMBL:GAP43670.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP43670.1};
RN [1] {ECO:0000313|EMBL:GAP43670.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP43670.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC 3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000764};
CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004816}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009473}.
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DR EMBL; DF968182; GAP43670.1; -; Genomic_DNA.
DR RefSeq; WP_062041158.1; NZ_DF968182.1.
DR AlphaFoldDB; A0A0S7C2M1; -.
DR STRING; 1678841.TBC1_111826; -.
DR PATRIC; fig|1678841.3.peg.2032; -.
DR OrthoDB; 9778711at2; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:InterPro.
DR CDD; cd00959; DeoC; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053091}.
SQ SEQUENCE 279 AA; 29999 MW; B419F241ECA665D8 CRC64;
MNKHHNFSPE VVAGQIAGIL ADPFKEFGSK HDAMRFALGI LDLTTLEGAD TKQKVEALCR
KAVSFSEKGL PNVAAVCVYP VFARQVHTLL EGTGIHTACV AGAFPAGQSP IHVKLAEVKY
AVEEGADEID MVISRGKLLE GEYIEVFDEI NAIKEVCGNV HLKVILETGE LTDLPRIYDA
SVIAMKAGGD FIKTSTGKIN PAATPEAAYV MLQAIRDYYE STGKITGFKP AGGISTPEQA
LVYVRLVESI LGPEWLNPVL FRIGASRLAD NLANELSGK
//